End user should determine optimal dilution for their particular applications and experiments.Western blot membranes were incubated with diluted antibody in 5% non-fat milk, PBS, 0.04% Tween20 for 1hour at room temperature.

Members of the Wiskott-Aldrich sydrome protein (WASP) family regulate the formation of actin-based cell structures in many cell types. These proteins contain C-terminal actin-binding domains that can stimulate actin polymerization. In addition, these proteins bind the ARP2/3 complex, which can nucleate actin polymerization at sites that lead to branched actin structures. WASP is expressed primarily in hematopoietic cells, while its homolog N-WASP is widely expressed. These proteins have 48% identity in human with the highest homology in the functional regions of these proteins. Serine and tyrosine phosphorylation regulates the activity of both proteins. WASP is observed as a 63 kDa protein in hematopoietic cells, while N-WASP is observed as a 65 kDa in many tissues, especially brain.

Background References

Baba, Y. et al. (1999) Blood 93:2003.

Higgs, H.N. & Pollard, T.D. (2001) Annu Rev Biochem 70:649-676.

Cory, G.O. et al. (2003) Mol Cell. 11(5):1229-39.

Immunogen

N-WASP synthetic peptide (coupled to KLH) corresponding to amino acid residues in the N-terminal region of human N-WASP. This N-WASP peptide sequence is 100% homologous to rat and mouse N-WASP, and has low homology to the corresponding region in the human WASP.

This antibody detects a 65 kDa* protein corresponding to the molecular mass of N-WASP on SDS-PAGE immunoblots of neonatal rat brain lysate. It is also detects 65 kDa* proteins in A431, human endothelial, and SKN-SH cells. It does not recognize the 63 kDa* WASP protein in Jurkat cell lysate.

*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.